Invertebrate defensins are a family of cysteine-rich antimicrobial peptides,
primarily active against Gram-positive bacteria. These defensins have been
found in arthropods (insects, ticks, spiders and scorpions), in bivalve
molluscs and in a fungus. These peptides range in length from 32 to 51 amino
acids. There are six conserved cysteines all involved in intrachain disulfide
bonds. A schematic representation of peptides from the invertebrate defensin
family is shown below.

We developed a profile that covers the whole structure of invertebrate
defensins.

Note:

Although low level sequence similarities have been reported [1]
between the invertebrate defensins and mammalian defensins, the topological
arrangement of the disulfide bonds as well as the tertiary structure [11] are
completely different in the two families.

Note:

Because historically these defensins were first found in insects and
scorpions, they used to be called arthropod defensin family or insect
defensins.

Last update:

May 2008 / Pattern removed, profile added and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
Prosite License
or see: prosite_license.html.